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5l1d

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<StructureSection load='5l1d' size='340' side='right' caption='[[5l1d]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
<StructureSection load='5l1d' size='340' side='right' caption='[[5l1d]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5l1d]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L1D FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5l1d]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L1D FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1d OCA], [http://pdbe.org/5l1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l1d RCSB], [http://www.ebi.ac.uk/pdbsum/5l1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1d ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1d OCA], [http://pdbe.org/5l1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l1d RCSB], [http://www.ebi.ac.uk/pdbsum/5l1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1d ProSAT]</span></td></tr>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
[[http://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN]] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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==See Also==
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*[[Ryanodine receptor|Ryanodine receptor]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]

Revision as of 08:58, 18 July 2018

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Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)

5l1d, resolution 10.50Å

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